An electrophoretically homogeneous preparation of endo-polygalacturonase (poly(1,4-α-d-galacturonide)glycanohydrolase, EC 3.2.1.15) from culture filtrates of Rhizoctonia fragariae, a pathogenic agent in strawberry plants, was resolved into two isoenzymes when subjected to isoelectrofocusing in a narrow pH range. The isoelectric points of the two isoenzymes were 6.76 ± 0.03 and 7.08 ± 0.05. The two polygalacturonases exhibited similar substrate specificity, pH optimum and pattern of degradation of sodium polypectate. The two enzymes consisted of a sigle polypeptide chain which had an apparent molecular weight of 36 000 as determined by gel filtration on Sephadex G-100
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
AbstractWe isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, ...
An electrophoretically homogeneous preparation of endo-polygalacturonase (poly(1,4-α-d-galacturonide...
A polygalacturonase from culture filtrates of a strain of Rhizopus stolonifer was purified about 80 ...
A pectinase was identified and isolated from a commercial Aspergillus niger pectinase preparation. T...
An endo-polygalacturonase secreted by Aspergillus sojae was characterized after being purified to ho...
The Gibberella fujikuroi complex includes toxigenic and pathogenic fungal species able to produce di...
The enzyme polygalacturonase from culture filtrates of Aspergillus was purified and classified as a...
The production of polygalacturonase during the deterioration of tomato (Lycopersicon esculentum Mil...
A polygalacturonase from the filamentous fungus Rhizopus oryzae strain sb (NRRL 29086), previously s...
Three polygalacturonases (PG) have been isolated from carrots (Daucus carota L. cv. Kintoki). Two we...
Five endo-polygalacturonases (PGs), three produced in culture filtrate by Fusarium moniliforme, Scle...
Sclerotium rolfsii (strain CBS 350.80) was found to produce extraordinary high amounts of polygalact...
The aim of this work was to study the purification and physicochemical properties of an endo-polygal...
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
AbstractWe isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, ...
An electrophoretically homogeneous preparation of endo-polygalacturonase (poly(1,4-α-d-galacturonide...
A polygalacturonase from culture filtrates of a strain of Rhizopus stolonifer was purified about 80 ...
A pectinase was identified and isolated from a commercial Aspergillus niger pectinase preparation. T...
An endo-polygalacturonase secreted by Aspergillus sojae was characterized after being purified to ho...
The Gibberella fujikuroi complex includes toxigenic and pathogenic fungal species able to produce di...
The enzyme polygalacturonase from culture filtrates of Aspergillus was purified and classified as a...
The production of polygalacturonase during the deterioration of tomato (Lycopersicon esculentum Mil...
A polygalacturonase from the filamentous fungus Rhizopus oryzae strain sb (NRRL 29086), previously s...
Three polygalacturonases (PG) have been isolated from carrots (Daucus carota L. cv. Kintoki). Two we...
Five endo-polygalacturonases (PGs), three produced in culture filtrate by Fusarium moniliforme, Scle...
Sclerotium rolfsii (strain CBS 350.80) was found to produce extraordinary high amounts of polygalact...
The aim of this work was to study the purification and physicochemical properties of an endo-polygal...
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polyg...
AbstractWe isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, ...